Andthe SARS-CoV-2from Codium fragile, against against SARS-CoV-2 virus infection (using siphonaxanthin pseudovirus) in HEK293/ SARS-CoV-2This study aims to supply helpful information for the application of marine ACE2 cells. virus infection (making use of the SARS-CoV-2 pseudovirus) in HEK293/ ACE2 cells. This study aims to supply helpful info for the application of marine carotenoids carotenoids beneficial to human overall health. advantageous to human wellness. two. Outcomes two. Results two.1. Molecular Docking 2.1. Molecular Docking Soon after visual inspection the top-ranked poses, the the potential binding websites were Right after visual inspection of in the top-ranked poses, prospective binding websites have been located located for the FX and SX models: the region correspondingbinding site in the SARS-CoV-2 for the FX and SX models: the area corresponding for the for the binding website of the SARSCoV-2 chimeric D4 Receptor Purity & Documentation receptor-binding (RBD) with ACE2 (Figure (Figure 1) binding binding chimeric receptor-binding domain domain (RBD) with ACE21) [23]. The [23]. Theenergies energies and residue interactions test the test compounds are presented in Table 1. The and residue interactions with all the withcompounds are presented in Table 1. The binding binding energies of FX and RBD have been -2.91 kcal/mol kcal/mol kcal/mol, respectively. energies of FX and SX for theSX for the RBD were -2.91 and -2.78and -2.78 kcal/mol, respectively. FXadisplayed a larger binding energy than SX, nevertheless it could the RBD-ACE2 FX displayed larger binding energy than SX, however it couldn’t bind at not bind in the RBD-ACE2 (Figure internet site (Figure 1A,B). hand, SX could bind at could bind at that location binding website binding1A,B). On the other Alternatively, SX that location (Figure 1A,C), (Figure 1A,C), energy was slightly reduce than FX. As shown in As shown in Figure two, but its bindingbut its binding power was slightly reduce than FX.Figure two, the potential the potential RBD with of RBD with HDAC7 web Ligands was hydrophobic the interacting residues interaction of interactionligands was hydrophobic in nature, and in nature, along with the interacting residues among RBD and to had been of ACE2 these of ACE2 (Tyr449, Tyr 489, and in between RBD and SX had been similarSX these related to(Tyr449, Tyr 489, and Gln 493), although Gln 493), towards the surface of RBD surface of RBD (Figure 2A). FX boundwhile FX bound towards the(Figure 2A).Figure 1. Surface and cartoon representations of structures of (A) the SARS-CoV-2 chimeric receptor-binding domain Figure 1. Surface cartoon representations of structures of (A) the SARS-CoV-2 chimeric receptor-binding domain (RBD) complexed (RBD) complexed with angiotensin-converting enzyme 22 (ACE2). The molecular docking poses (B)(B) fucoxanthin and angiotensin-converting enzyme (ACE2). The molecular docking poses of of fucoxanthin and (C) siphonaxanthin interacting with RBD (PDB:6vw1) analyzed with AutoDock Vina. The tertiary structures of RBD-ligands (C) siphonaxanthin interacting with RBD (PDB:6vw1) analyzed with AutoDockVina. The tertiary structures of RBD-ligands were produced with PyMOL. Ligands and ACE2 are depicted as green sticks and green cartoons, and the binding site residues had been made with PyMOL. Ligands and ACE2 are depicted as green sticks and green cartoons, as well as the binding website residues are labeled accordingly. are labeled accordingly.Int. J. Mol. Sci. 2021, 22,3 ofTable 1. Interaction and binding power of ligands with SARS-CoV-2 chimeric receptor-binding domain (RBD) in silico. SARS-CoV-2 Chimeric Receptor-Binding.
